| IED ID | IndEnz0005000795 |
| Enzyme Type ID | lipase000795 |
| Protein Name |
Platelet-activating factor acetylhydrolase IB subunit alpha1 EC 3.1.1.47 PAF acetylhydrolase 29 kDa subunit PAF-AH 29 kDa subunit PAF-AH subunit gamma PAFAH subunit gamma Platelet-activating factor acetylhydrolase alpha 1 subunit PAF-AH alpha 1 |
| Gene Name | Pafah1b3 Pafahg |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAP |
| Enzyme Length | 232 |
| Uniprot Accession Number | O35263 |
| Absorption | |
| Active Site | ACT_SITE 48; /evidence=ECO:0000250|UniProtKB:Q29460; ACT_SITE 193; /evidence=ECO:0000250|UniProtKB:Q29460; ACT_SITE 196; /evidence=ECO:0000250|UniProtKB:Q29460 |
| Activity Regulation | ACTIVITY REGULATION: Beta subunit (PAFAH1B1) inhibits the acetylhydrolase activity of the alpha1/alpha1 catalytic homodimer. {ECO:0000250|UniProtKB:Q29460}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9660828};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9660828};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + acetate + H(+); Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; Evidence={ECO:0000250|UniProtKB:Q29460};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; Evidence={ECO:0000250|UniProtKB:Q29460}; |
| DNA Binding | |
| EC Number | 3.1.1.47 |
| Enzyme Function | FUNCTION: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:9660828). The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain (By similarity). {ECO:0000250|UniProtKB:Q29460, ECO:0000269|PubMed:9660828}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Initiator methionine (1); Modified residue (2); Region (1) |
| Keywords | Acetylation;Cytoplasm;Hydrolase;Lipid degradation;Lipid metabolism;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:Q15102; MOD_RES 2; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q15102 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10940388; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,863 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17777; RHEA:17778; RHEA:40479; RHEA:40480; RHEA:41704; RHEA:41705 |
| Cross Reference Brenda | 3.1.1.47; |